Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P26883 (FKB1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A

Short name=PPIase FKBP1A
EC=5.2.1.8
Alternative name(s):
12 kDa FK506-binding protein
Short name=12 kDa FKBP
Short name=FKBP-12
Calstabin-1
FK506-binding protein 1A
Short name=FKBP-1A
Immunophilin FKBP12
Rotamase
Gene names
Name:Fkbp1a
Synonyms:Fkbp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length108 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides By similarity.

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulation

Inhibited by both FK506 and rapamycin.

Subunit structure

Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation By similarity. Interacts with ACVR1B and SMAD7. Interacts directly with RYR1, RYR2 and RYR3 By similarity. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Ref.6

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP1 subfamily.

Contains 1 PPIase FKBP-type domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Rotamase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSMAD protein complex assembly

Inferred from electronic annotation. Source: Ensembl

T cell proliferation

Inferred from mutant phenotype PubMed 14605212. Source: MGI

beta-amyloid formation

Inferred from electronic annotation. Source: Ensembl

cytokine-mediated signaling pathway

Inferred from mutant phenotype PubMed 14605212. Source: MGI

extracellular fibril organization

Inferred from electronic annotation. Source: Ensembl

heart morphogenesis

Inferred from mutant phenotype PubMed 9461216. Source: BHF-UCL

heart trabecula formation

Inferred from mutant phenotype PubMed 9461216. Source: BHF-UCL

muscle contraction

Inferred from mutant phenotype PubMed 15289441. Source: MGI

negative regulation of protein phosphatase type 2B activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 15467718. Source: MGI

peptidyl-proline modification

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: UniProtKB-KW

protein peptidyl-prolyl isomerization

Inferred from Biological aspect of Ancestor. Source: GOC

regulation of activin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of immune response

Inferred from electronic annotation. Source: Ensembl

regulation of ryanodine-sensitive calcium-release channel activity

Inferred from mutant phenotype PubMed 9461216. Source: BHF-UCL

release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 12704193. Source: MGI

response to caffeine

Inferred from mutant phenotype PubMed 15289441. Source: MGI

response to iron ion

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle tissue morphogenesis

Inferred from mutant phenotype PubMed 9461216. Source: BHF-UCL

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

axon

Inferred from Biological aspect of Ancestor. Source: RefGenome

axon terminus

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from Biological aspect of Ancestor. Source: RefGenome

membrane

Inferred from direct assay PubMed 12704193. Source: MGI

sarcoplasmic reticulum membrane

Inferred from direct assay PubMed 14592808. Source: MGI

   Molecular_functionFK506 binding

Inferred from direct assay Ref.1. Source: MGI

drug binding

Inferred from direct assay PubMed 15467718. Source: MGI

ion channel binding

Inferred from physical interaction PubMed 19198614. Source: BHF-UCL

peptidyl-prolyl cis-trans isomerase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1A
PRO_0000075290

Regions

Domain20 – 10889PPIase FKBP-type

Amino acid modifications

Modified residue21N-acetylglycine By similarity
Modified residue91Phosphoserine By similarity
Modified residue531N6-acetyllysine; alternate Ref.7
Modified residue531N6-succinyllysine; alternate Ref.7

Sequences

Sequence LengthMass (Da)Tools
P26883 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8C265ED5803F6987

FASTA10811,923
        10         20         30         40         50         60 
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT LGKQEVIRGW 

        70         80         90        100 
EEGVAQMSVG QRAKLIISSD YAYGATGHPG IIPPHATLVF DVELLKLE 

« Hide

References

« Hide 'large scale' references
[1]"cDNA encoding murine FK506-binding protein (FKBP): nucleotide and deduced amino acid sequence."
Nelson P.A., Lippke J.A., Murcko M.A., Rosborough S.L., Peattie D.A.
Gene 109:255-258(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
[2]Shou W., Bao S., Mathews L.S., Matzuk M.M.
Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 129/Sv.
[3]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ILS and ISS.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Hippocampus.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[6]"Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; RYR1 AND PROTEIN PHOSPHATASE 1.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60203 mRNA. Translation: CAA42762.1.
U65100, U65098, U65099 Genomic DNA. Translation: AAB17554.1.
AF483488 mRNA. Translation: AAL90762.1.
AF483489 mRNA. Translation: AAL90763.1.
AK002777 mRNA. Translation: BAB22351.1.
AK010693 mRNA. Translation: BAB27125.1.
AK019362 mRNA. Translation: BAB31680.1.
AK154751 mRNA. Translation: BAE32804.1.
AK168333 mRNA. Translation: BAE40271.1.
AK169186 mRNA. Translation: BAE40963.1.
AK169242 mRNA. Translation: BAE41008.1.
BC004671 mRNA. Translation: AAH04671.1.
PIRJH0528.
RefSeqNP_032045.1. NM_008019.2.
XP_006498811.1. XM_006498748.1.
UniGeneMm.278458.
Mm.487732.

3D structure databases

ProteinModelPortalP26883.
SMRP26883. Positions 2-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199682. 2 interactions.
DIPDIP-29707N.
IntActP26883. 3 interactions.
MINTMINT-4095099.

PTM databases

PhosphoSiteP26883.

Proteomic databases

PaxDbP26883.
PRIDEP26883.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044011; ENSMUSP00000037206; ENSMUSG00000032966.
GeneID14225.
KEGGmmu:14225.
UCSCuc008ndy.1. mouse.

Organism-specific databases

CTD2280.
MGIMGI:95541. Fkbp1a.

Phylogenomic databases

eggNOGCOG0545.
GeneTreeENSGT00550000074272.
HOGENOMHOG000154887.
HOVERGENHBG051623.
KOK09568.
OMAGYLYDES.
OrthoDBEOG7ZGX5T.
TreeFamTF105291.

Gene expression databases

ArrayExpressP26883.
BgeeP26883.
CleanExMM_FKBP1A.
GenevestigatorP26883.

Family and domain databases

InterProIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERPTHR10516. PTHR10516. 1 hit.
PfamPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285479.
PROP26883.
SOURCESearch...

Entry information

Entry nameFKB1A_MOUSE
AccessionPrimary (citable) accession number: P26883
Secondary accession number(s): Q545E9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot